Thyroxine binding properties of glycosylated human serum albumin as measured by fluorescence.

Abstract:

:Thyroid hormone, thyroxine (T4) binding to glycosylated human serum albumin (G-HSA), and native human serum albumin (HSA) were studied as a function of pH using the fluorescence method. T4 binding affinity for G-HSA was remarkably reduced in an alkaline pH as compared with the native HSA. The thermodynamic parameters for binding are estimated at pH 7.5: (a) for G-HSA, delta G = -8.50 +/- 0.04 kcal mol-1 (30 degrees C), delta H = -5.2 kcal mol-1, delta S = +11 e.u.; (b) for HSA, delta G = -8.89 +/- 0.04 kcal mol-1 (30 degrees C), delta H = -3.5 kcal mol-1, delta S = +18 e.u. These results suggest that the glycosylation of HSA causes a variation in the electrostatic interaction between T4 and HSA.

journal_name

Biol Pharm Bull

authors

Okabe N,Yoshida S

doi

10.1248/bpb.18.154

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

154-5

issue

1

eissn

0918-6158

issn

1347-5215

journal_volume

18

pub_type

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